Evidence map›Paper›PMID 42733066›Full record

ArticleNature communications2026

USP5 acts as a proteolytic switch to control SDE2 function via UBL-directed cleavage.

Liam T Hales, Paul M Tammiste, Adam J Walker, Rebecca Bryce, Andrew Sugden, Axel Knebel, Rachel Toth, Frédéric Lamoliatte, Marian Péteri, Oliwia Curry and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Liam T Hales *MRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, Faculty of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0009-0009-7870-2671
Paul M Tammiste *MRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, Faculty of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0009-0008-8000-5341
Adam J WalkerMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, Faculty of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0009-0002-3563-1809
Rebecca BryceMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, Faculty of Life Sciences, University of Dundee, Dundee, UK.
Andrew SugdenMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, Faculty of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0009-0008-2015-2737
Axel KnebelMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, Faculty of Life Sciences, University of Dundee, Dundee, UK.
Rachel TothMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, Faculty of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0002-1337-0612
Frédéric LamoliatteMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, Faculty of Life Sciences, University of Dundee, Dundee, UK.
Marian PéteriMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, Faculty of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0003-2211-6189
Oliwia CurrySchool of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne, UK.ORCID http://orcid.org/0000-0001-7471-3685
Glenn R MassonDivision of Cancer Research, Faculty of Health, University of Dundee, Ninewells Hospital, Dundee, UK.ORCID http://orcid.org/0000-0002-1386-4719
Virginia De CesareMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, Faculty of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0002-2640-6389
Chiara ManiaciMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, Faculty of Life Sciences, University of Dundee, Dundee, UK. cmaniaci001@dundee.ac.uk.ORCID http://orcid.org/0000-0001-7887-7388

Funding

RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/T009454/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/V019635/1RCUK | Engineering and Physical Sciences Research Council (EPSRC) EP/S022791/1RCUK | Medical Research Council (MRC) MC_ST_00038Royal Society RGS\R2\212269Royal Society URF\R1\231436University of Dundee (Dundee University) Baxter Fellowship
6 · The paper itself

Abstract

Proteolytic processing is a fundamental regulatory mechanism in eukaryotic cells, yet the molecular identities and mechanisms underlying such events are often poorly defined. Silencing Defective 2 (SDE2), an essential human protein, plays important roles in mRNA splicing, DNA repair and ribosomal biogenesis. Cleavage of SDE2 downstream to its N-terminal ubiquitin-like domain (SDE2

Indexed as

EndopeptidasesUbiquitinCarrier ProteinsHEK293 CellsHeLa CellsHumansProtein DomainsProteolysisRNA SplicingCarrier ProteinsEndopeptidasesUbap2L protein, humanUbiquitin

Identifiers

PMID42733066
PMCPMC13572447

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.